PLI2A_ARATH
ID PLI2A_ARATH Reviewed; 226 AA.
AC O80839; F4IH47;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 136.
DE RecName: Full=LIM domain-containing protein PLIM2a {ECO:0000305};
DE AltName: Full=Pollen-expressed LIM protein 2 {ECO:0000303|PubMed:11085265};
DE Short=AtPLIM2;
GN Name=PLIM2A {ECO:0000303|PubMed:17573466};
GN Synonyms=PLIM2 {ECO:0000303|PubMed:11085265};
GN OrderedLocusNames=At2g45800 {ECO:0000312|Araport:AT2G45800};
GN ORFNames=F4I18.22 {ECO:0000312|EMBL:AAC28544.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=11085265; DOI=10.1007/s004380000312;
RA Eliasson A., Gass N., Mundel C., Baltz R., Kraeuter R., Evrard J.L.,
RA Steinmetz A.;
RT "Molecular and expression analysis of a LIM protein gene family from
RT flowering plants.";
RL Mol. Gen. Genet. 264:257-267(2000).
RN [6]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=17573466; DOI=10.1093/dnares/dsm013;
RA Arnaud D., Dejardin A., Leple J.C., Lesage-Descauses M.C., Pilate G.;
RT "Genome-wide analysis of LIM gene family in Populus trichocarpa,
RT Arabidopsis thaliana, and Oryza sativa.";
RL DNA Res. 14:103-116(2007).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=17905860; DOI=10.1104/pp.107.104422;
RA Alves-Ferreira M., Wellmer F., Banhara A., Kumar V., Riechmann J.L.,
RA Meyerowitz E.M.;
RT "Global expression profiling applied to the analysis of Arabidopsis stamen
RT development.";
RL Plant Physiol. 145:747-762(2007).
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP F-ACTIN.
RX PubMed=20817848; DOI=10.1105/tpc.110.075960;
RA Papuga J., Hoffmann C., Dieterle M., Moes D., Moreau F., Tholl S.,
RA Steinmetz A., Thomas C.;
RT "Arabidopsis LIM proteins: a family of actin bundlers with distinct
RT expression patterns and modes of regulation.";
RL Plant Cell 22:3034-3052(2010).
CC -!- FUNCTION: Binds to actin filaments and promotes cross-linking into
CC thick bundles. Has an actin-stabilizing activity. The actin regulatory
CC activities are inhibited by pH > 6.8 but are [Ca(2+)] independent.
CC {ECO:0000269|PubMed:20817848}.
CC -!- SUBUNIT: Interacts with F-actin. {ECO:0000269|PubMed:20817848}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:20817848}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O80839-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O80839-2; Sequence=VSP_056811;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in flowers, in the tapetum
CC and in pollen grains. Detected in leaves and stems.
CC {ECO:0000269|PubMed:11085265, ECO:0000269|PubMed:17905860,
CC ECO:0000269|PubMed:20817848}.
CC -!- MISCELLANEOUS: Cross-links actin with a constant of dissociation of 1.3
CC uM. {ECO:0000269|PubMed:20817848}.
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DR EMBL; AC004665; AAC28544.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10602.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10603.1; -; Genomic_DNA.
DR EMBL; AK118044; BAC42675.1; -; mRNA.
DR EMBL; BT005586; AAO64006.1; -; mRNA.
DR PIR; T02467; T02467.
DR RefSeq; NP_001031545.1; NM_001036468.2. [O80839-2]
DR RefSeq; NP_182104.1; NM_130143.4. [O80839-1]
DR AlphaFoldDB; O80839; -.
DR BioGRID; 4524; 6.
DR IntAct; O80839; 6.
DR STRING; 3702.AT2G45800.1; -.
DR PaxDb; O80839; -.
DR PRIDE; O80839; -.
DR ProteomicsDB; 236166; -. [O80839-1]
DR EnsemblPlants; AT2G45800.1; AT2G45800.1; AT2G45800. [O80839-1]
DR EnsemblPlants; AT2G45800.2; AT2G45800.2; AT2G45800. [O80839-2]
DR GeneID; 819188; -.
DR Gramene; AT2G45800.1; AT2G45800.1; AT2G45800. [O80839-1]
DR Gramene; AT2G45800.2; AT2G45800.2; AT2G45800. [O80839-2]
DR KEGG; ath:AT2G45800; -.
DR Araport; AT2G45800; -.
DR TAIR; locus:2050735; AT2G45800.
DR eggNOG; KOG1700; Eukaryota.
DR HOGENOM; CLU_026811_1_0_1; -.
DR InParanoid; O80839; -.
DR OMA; GRCQKTV; -.
DR PhylomeDB; O80839; -.
DR PRO; PR:O80839; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O80839; baseline and differential.
DR Genevisible; O80839; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0051015; F:actin filament binding; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051017; P:actin filament bundle assembly; IDA:TAIR.
DR InterPro; IPR045268; LIMA-like.
DR InterPro; IPR001781; Znf_LIM.
DR PANTHER; PTHR24206; PTHR24206; 1.
DR Pfam; PF00412; LIM; 2.
DR SMART; SM00132; LIM; 2.
DR PROSITE; PS00478; LIM_DOMAIN_1; 1.
DR PROSITE; PS50023; LIM_DOMAIN_2; 2.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; Cytoplasm; Cytoskeleton; LIM domain;
KW Metal-binding; Reference proteome; Repeat; Zinc.
FT CHAIN 1..226
FT /note="LIM domain-containing protein PLIM2a"
FT /id="PRO_0000430595"
FT DOMAIN 8..68
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 104..164
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT REGION 173..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..210
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..226
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..45
FT /note="MSFTGTLDKCKACDKTVYVMDLLTLEGNTYHKSCFRCTHCKGTLV -> MLH
FT CFKRPHLFLTQ (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_056811"
SQ SEQUENCE 226 AA; 24943 MW; A1017098C3E58E42 CRC64;
MSFTGTLDKC KACDKTVYVM DLLTLEGNTY HKSCFRCTHC KGTLVISNYS SMDGVLYCKP
HFEQLFKESG NYSKNFQAGK TEKPNDHLTR TPSKLSSFFS GTQDKCATCK KTVYPLEKVT
MEGESYHKTC FRCTHSGCPL THSSYASLNG VLYCKVHFNQ LFLEKGSYNH VHQAAANHRR
SASSGGASPP SDDHKPDDTA SIPEAKEDDA APEAAGEEEP EPVVES
